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-Chain and a Lymphoid Cell Environment1
Department of Microbiology and Immunology, University of Miami School of Medicine, Miami, FL 33136
The common 
-chain (c), a subunit of the IL-2R, is essential
for high affinity ligand binding and signal transduction due to Jak3
association to c. Another consequence of IL-2/IL-2R interaction is
rapid receptor-mediated endocytosis of the receptor-ligand complex. In
the present study, we establish that this rapid endocytosis of IL-2 in
a T cell tumor line is dependent upon the cytoplasmic tail of c.
Deletion mutants of the cytoplasmic tail mapped this activity to 9 aa
of c, 45–54 aa distal to the transmembrane region. In contrast,
ligand-independent constitutive endocytosis of c occurred more
slowly and was dependent upon a PEST sequence in a more
membrane-proximal region of the cytoplasmic tail of c. Thus, this
receptor subunit may use distinct sorting signals for its constitutive
regulation and ligand-induced endocytosis. Rapid endocytosis of IL-2
was inhibited by the tyrosine kinase inhibitor genistein, implicating a
role for a signal transduction pathway in IL-2 internalization.
However, one T cell line bearing a mutant c exhibited impaired
endocytosis of IL-2, despite normal IL-2-induced Jak/STAT activation.
Furthermore, inefficient endocytosis of IL-2 was noted after
transfection of the COS7 epithelial cell line with the IL-2R, and
further reconstitution of these cells with Jak/STAT proteins did not
enhance this internalization. Collectively, these latter findings
indicate that rapid endocytosis of IL-2 is dependent upon cellular
signaling in lymphoid cell environment that is not solely a consequence
of the presence of the Jak/STAT pathway.
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